A linker peptide with high affinity towards silica-containing materials

Anwar Sunna, Fei Chi, Peter L. Bergquist

Research output: Contribution to journalArticleResearchpeer-review

Abstract

A peptide sequence with affinity to silica-containing materials was fused to a truncated form of Streptococcus strain G148 Protein G. The resulting recombinant Linker-Protein G (LPG) was produced in Escherichia coli and purified to apparent homogeneity. It displayed high affinity towards two natural clinoptilolite zeolites. The LPG also displayed high binding affinity towards commercial-grade synthetic zeolite, silica and silica-containing materials. A commercial sample of the truncated Protein G and a basic protein, both without the linker, did not bind to natural or synthetic zeolites or silica. We conclude that the zeolite-binding affinity is mediated by the linker peptide sequence. As a consequence, these data may imply that the binding affinity is directed to the SiO2 component rather than to the atomic orientation on the zeolite crystal surface as previously assumed.

LanguageEnglish
Pages485-492
Number of pages8
JournalNew Biotechnology
Volume30
Issue number5
DOIs
Publication statusPublished - 25 Jun 2013

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Zeolites
Silicon Dioxide
Peptides
Silica
Proteins
Recombinant proteins
Crystal orientation
Escherichia coli
Streptococcus
Recombinant Proteins
Crystals

Cite this

Sunna, Anwar ; Chi, Fei ; Bergquist, Peter L. / A linker peptide with high affinity towards silica-containing materials. In: New Biotechnology. 2013 ; Vol. 30, No. 5. pp. 485-492.
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A linker peptide with high affinity towards silica-containing materials. / Sunna, Anwar; Chi, Fei; Bergquist, Peter L.

In: New Biotechnology, Vol. 30, No. 5, 25.06.2013, p. 485-492.

Research output: Contribution to journalArticleResearchpeer-review

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